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Pregled bibliografske jedinice broj: 752200

Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom


Leonardi, Adrijana; Sajević, Tamara; Latinović, Zorica; Pungercar, Joze; Lang Balija, Maja; Trampus Bakija, Alenka; Vidmar, Robert; Halassy, Beata; Krizaj, Igor
Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom // Biochimie, 109 (2015), 78-87 doi:10.1016/j.biochi.2014.12.013 (međunarodna recenzija, članak, znanstveni)


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Naslov
Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom

Autori
Leonardi, Adrijana ; Sajević, Tamara ; Latinović, Zorica ; Pungercar, Joze ; Lang Balija, Maja ; Trampus Bakija, Alenka ; Vidmar, Robert ; Halassy, Beata ; Krizaj, Igor

Izvornik
Biochimie (0300-9084) 109 (2015); 78-87

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Metalloproteinase; Serotherapy; Snake venom; Vipera ammodytes ammodytes; alpha-Fibrinogenase

Sažetak
A high molecular mass metalloproteinase with alpha-fibrinogenolytic activity, termed VaF1, was purified from nose-horned viper (Vipera ammodytes ammodytes) venom. Subcutaneous injection of 9mug of VaF1 did not induce bleeding in rats. Nevertheless, invitro it degraded collagen IV, nidogen and fibronectin, components of the extracellular matrix, although with low efficacy and narrow specificity. VaF1 would be expected to exert anti-coagulant action, due to its hydrolysis of fibrinogen, factor X, prothrombin and plasminogen, plasma proteins involved in blood coagulation. The enzyme is a single-chain glycoprotein with a molecular mass of 49.7kDa, as determined by mass spectrometry, and multiple isoelectric points centred at pH 5.8. The complete amino acid sequence of the precursor of VaF1 was deduced by cloning and sequencing its cDNA. Composed of metalloproteinase, disintegrin-like and cysteine-rich domains, VaF1 is a typical P-IIIa subclass snake venom metalloproteinase. Although it possesses a collagen-binding sequence in its disintegrin-like domain, VaF1 displayed no effect on collagen-induced platelet aggregation invitro. Two consensus N-glycosylation sites are present in the sequence of VaF1, however, the extent of its glycosylation is low, only 5.2% of the total molecular mass. Interestingly, in standard experimental conditions VaF1 is not recognised by antiserum against the whole venom, so it can contribute to post-serotherapy complications, such as ineffective blood coagulation, in the envenomed patient.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Temeljne medicinske znanosti



POVEZANOST RADA


Projekti:
021-0212432-2033 - Imunogeničnost komponenti kompleksnih antigena (Halassy, Beata, MZOS ) ( CroRIS)

Ustanove:
Imunološki zavod d.d.,
Sveučilište u Zagrebu

Profili:

Avatar Url Maja Lang Balija (autor)

Avatar Url Beata Halassy (autor)

Poveznice na cjeloviti tekst rada:

doi www.sciencedirect.com dx.doi.org

Citiraj ovu publikaciju:

Leonardi, Adrijana; Sajević, Tamara; Latinović, Zorica; Pungercar, Joze; Lang Balija, Maja; Trampus Bakija, Alenka; Vidmar, Robert; Halassy, Beata; Krizaj, Igor
Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom // Biochimie, 109 (2015), 78-87 doi:10.1016/j.biochi.2014.12.013 (međunarodna recenzija, članak, znanstveni)
Leonardi, A., Sajević, T., Latinović, Z., Pungercar, J., Lang Balija, M., Trampus Bakija, A., Vidmar, R., Halassy, B. & Krizaj, I. (2015) Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom. Biochimie, 109, 78-87 doi:10.1016/j.biochi.2014.12.013.
@article{article, author = {Leonardi, Adrijana and Sajevi\'{c}, Tamara and Latinovi\'{c}, Zorica and Pungercar, Joze and Lang Balija, Maja and Trampus Bakija, Alenka and Vidmar, Robert and Halassy, Beata and Krizaj, Igor}, year = {2015}, pages = {78-87}, DOI = {10.1016/j.biochi.2014.12.013}, keywords = {Metalloproteinase, Serotherapy, Snake venom, Vipera ammodytes ammodytes, alpha-Fibrinogenase}, journal = {Biochimie}, doi = {10.1016/j.biochi.2014.12.013}, volume = {109}, issn = {0300-9084}, title = {Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom}, keyword = {Metalloproteinase, Serotherapy, Snake venom, Vipera ammodytes ammodytes, alpha-Fibrinogenase} }
@article{article, author = {Leonardi, Adrijana and Sajevi\'{c}, Tamara and Latinovi\'{c}, Zorica and Pungercar, Joze and Lang Balija, Maja and Trampus Bakija, Alenka and Vidmar, Robert and Halassy, Beata and Krizaj, Igor}, year = {2015}, pages = {78-87}, DOI = {10.1016/j.biochi.2014.12.013}, keywords = {Metalloproteinase, Serotherapy, Snake venom, Vipera ammodytes ammodytes, alpha-Fibrinogenase}, journal = {Biochimie}, doi = {10.1016/j.biochi.2014.12.013}, volume = {109}, issn = {0300-9084}, title = {Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom}, keyword = {Metalloproteinase, Serotherapy, Snake venom, Vipera ammodytes ammodytes, alpha-Fibrinogenase} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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